3.4.21.12	Eglin c	very effective inhibitor	2653	
3.4.21.12	Eglin c	-	2653	
3.4.21.12	guanidine hydrochloride	1% residual activity in the presence of 4 mM guanidine hydrochloride	1048	
3.4.21.12	methoxysuccinyl-Ala-Ala-Pro-L-boroPhe	the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates close to tetrahedral boron coordination in the active site of the enzyme/inhibitor complex	117726	
3.4.21.12	methoxysuccinyl-Ala-Ala-Pro-L-boroVal	the carboxylate of the C-terminal amino acid residue is replaced with B(OH)2. Boron-11 pure quadrupole resonance investigation indicates tetrahedral boron coordination in the active site of the enzyme/inhibitor complex	117725	
3.4.21.12	additional information	-	2	
3.4.21.12	additional information	mechanism	2	
3.4.21.12	additional information	lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility of the histidine residue and the enzyme's catalytic activity	2	
3.4.21.12	N-terminal 166 amino acid Pro region of alpha-lytic protease	dual role of folding and inhibition	101143	
3.4.21.12	N-Tert-butyloxycarbonylalanylpropylvaline boronic acid	-	46343